Immobilization of Enzymes on a Phospholipid Bionically Modified Polysulfone Gradient-Pore Membrane for the Enhanced Performance of Enzymatic Membrane Bioreactors

• Published in: Molecules (Basel, Switzerland) Switzerland), 2018-01, Vol.23 (1), p.144
• Main Authors: Guo, Yizong, Zhu, Xueyan, Fang, Fei, Hong, Xiao, Wu, Huimin, Chen, Dajing, Huang, Xiaojun
• Format: Article
• Language: English
• Subjects: Apertures; Biological activity; biomimetic interfaces; Biomimetics; Bioreactors; Catalysis; Circular dichroism; Dichroism; Enzymatic activity; Enzymes; Enzymes, Immobilized - chemistry; Fluxes; Glycerol; gradient-pore membrane; Hollow fiber membranes; Immobilization; Leaching; Lecithin; Lecithins - chemistry; Lipase; membrane bioreactors; Membranes, Artificial; Micelles; Phospholipids; Phospholipids - chemistry; Polymers - chemistry; Porosity; Spectroscopy; Spectroscopy, Fourier Transform Infrared; Sulfones - chemistry; Surface-Active Agents - chemistry
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules23010144

Enzymatic membrane bioreactors (EMBRs), with synergistic catalysis-separation performance, have increasingly been used for practical applications. Generally, the membrane properties, particularly the pore structures and interface interactions, have a significant impact on the catalytic efficiency of the EMBR. Therefore, a biomimetic interface based on a phospholipid assembled onto a polysulfone hollow-fiber membrane with perfect radial gradient pores (RGM-PSF) has been prepared in this work to construct a highly efficient and stable EMBR. On account of the special pore structure of the RGM-PSF with the apertures decreasing gradually from the inner side to the outer side, the enzyme molecules could be evenly distributed on the three-dimensional skeleton of the membrane. In addition, the supported phospholipid layer in the membrane, prepared by physical adsorption, was used for the immobilization of the enzymes, which provides sufficient linkage to prevent the enzymes from leaching but also accommodates as many enzyme molecules as possible to retain high bioactivity. The properties of the EMBR were studied by using lipase from for the hydrolysis of glycerol triacetate as a model. Energy-dispersive X-ray and circular dichroism spectroscopy were employed to observe the effect of lecithin on the membrane and structure changes in the enzyme, respectively. The operational conditions were investigated to optimize the performance of the EMBR by testing substrate concentrations from 0.05 to 0.25 M, membrane fluxes from 25.5 to 350.0 L·m ·h , and temperatures from 15 to 55 °C. As a result, the obtained EMBR showed a desirable performance with 42% improved enzymatic activity and 78% improved catalytic efficiency relative to the unmodified membrane.